ID A0A3B4CH27_PYGNA Unreviewed; 899 AA.
AC A0A3B4CH27;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000552};
DE EC=2.7.11.13 {ECO:0000256|PIRNR:PIRNR000552};
GN Name=PRKD3 {ECO:0000313|Ensembl:ENSPNAP00000010131.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000010131.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000010131.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13; Evidence={ECO:0000256|ARBA:ARBA00000569,
CC ECO:0000256|PIRNR:PIRNR000552};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000552};
CC -!- ACTIVITY REGULATION: Activated by DAG and phorbol esters.
CC {ECO:0000256|PIRNR:PIRNR000552}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000552}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. PKD subfamily. {ECO:0000256|ARBA:ARBA00008582}.
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DR RefSeq; XP_017567361.1; XM_017711872.1.
DR AlphaFoldDB; A0A3B4CH27; -.
DR STRING; 42514.ENSPNAP00000010131; -.
DR Ensembl; ENSPNAT00000016718.1; ENSPNAP00000010131.1; ENSPNAG00000015710.1.
DR GeneID; 108435798; -.
DR CTD; 23683; -.
DR GeneTree; ENSGT00950000183024; -.
DR OMA; NERFITH; -.
DR OrthoDB; 2939922at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004697; F:diacylglycerol-dependent serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0048468; P:cell development; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20841; C1_PKD3_rpt1; 1.
DR CDD; cd20844; C1_PKD3_rpt2; 1.
DR CDD; cd01239; PH_PKD; 1.
DR CDD; cd14082; STKc_PKD; 1.
DR Gene3D; 3.30.60.20; -; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR22968; PROTEIN KINASE C, MU; 1.
DR PANTHER; PTHR22968:SF26; SERINE_THREONINE-PROTEIN KINASE D3; 1.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000552; PKC_mu_nu_D2; 1.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000552};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR000552};
KW Kinase {ECO:0000256|PIRNR:PIRNR000552};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000552};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000552};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000552};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000552};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000552};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 157..207
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 274..324
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 420..539
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 585..841
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 708
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-1"
FT BINDING 591..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000552-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 899 AA; 101283 MW; F9F95D365E14AB74 CRC64;
MSACSSTTPL TPLPKAYLHS QHPPTPPTPS PSPSPPVALY HRLSNGSHSA PSPTLSRGSL
HGVSFLLQIG LTRETVNLEA PDLSLNAVKD LVCSIIDQKF PECGFFGMYD KILLFRHDLN
SDNILQRLTS AEDIHEGDLI EVVLSAQATV EDFQIRPHAL YVHSYKAPTF CDYCGEMLWG
LVRQGLKCEG CGLNYHKRCA FKIPNNCSGV RKRRLSNVSL PGPSLSVPRP LPAEHSVVNL
DEQRSHQEAG KRIPSWSGRP IWMEKMVLGR VKVPHTFVIH TYTRPTICQY CKRLLKGLFR
QGMQCKDCKF NCHKRCASKV PKDCLGEVLF NGEPASPGPD SDTTMEVDSS DVNSDSSRVL
DDSEEPTTPD DKIFQGYPFT DQESNEEAVK TPQISPSTST NIPLMRVVQS IKHTKRRSST
VVKEGWMVHY TSRDNLRKRH YWRLDSKSLT LFQNDSGAKF YKEIPLSEIL QVEAAQDFGS
LALGSNPHCF EIITATMVYY VGENMGGPHL HIHNPMLAAS GVGLEVAQSW EKAIRQALMP
VPVTPQPSVG SAAGQGKDHK DLSISISVSN SQIQENVDIS SVYQIFADEV LGSGQFGIVY
GGKHRKTGRD VAIKVIDKMR FPTKQESQLR NEVAILQNLH HPGIVNLECM FETPERVFVV
MEKLHGDMLE MILSSEKSRL PERITKFLVT QILVALRHLH FKNIVHCDLK PENVLLASAE
PFPQVKLCDF GFARIIGEKS FRRSVVGTPA YLAPEVLRSK GYNRSLDMWS VGVIIYVSLS
GTFPFNEDED INDQIQNAAF MYPPMPWKEI STEATDLINN LLQVKMRKRY SVDKSLSHPW
LQDYQTWLDL REFETRRGER YITHESDDAR WEEYADEHSL IYPKHFIMAP NLDDMDEDP
//
